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Database: UniProt
Entry: G7ZGW5_AZOL4
LinkDB: G7ZGW5_AZOL4
Original site: G7ZGW5_AZOL4 
ID   G7ZGW5_AZOL4            Unreviewed;       164 AA.
AC   G7ZGW5;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 56.
DE   SubName: Full=Thioredoxin {ECO:0000313|EMBL:CBS90567.1};
GN   Name=trxC {ECO:0000313|EMBL:CBS90567.1};
GN   OrderedLocusNames=AZOLI_p40170 {ECO:0000313|EMBL:CBS90567.1};
OS   Azospirillum lipoferum (strain 4B).
OG   Plasmid AZO_p4 {ECO:0000313|EMBL:CBS90567.1,
OG   ECO:0000313|Proteomes:UP000005667}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=862719 {ECO:0000313|EMBL:CBS90567.1, ECO:0000313|Proteomes:UP000005667};
RN   [1] {ECO:0000313|Proteomes:UP000005667}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4B {ECO:0000313|Proteomes:UP000005667};
RC   PLASMID=Plasmid AZO_p4 {ECO:0000313|Proteomes:UP000005667};
RX   PubMed=22216014; DOI=10.1371/journal.pgen.1002430;
RA   Wisniewski-Dye F., Borziak K., Khalsa-Moyers G., Alexandre G.,
RA   Sukharnikov L.O., Wuichet K., Hurst G.B., McDonald W.H., Robertson J.S.,
RA   Barbe V., Calteau A., Rouy Z., Mangenot S., Prigent-Combaret C.,
RA   Normand P., Boyer M., Siguier P., Dessaux Y., Elmerich C., Condemine G.,
RA   Krishnen G., Kennedy I., Paterson A.H., Gonzalez V., Mavingui P.,
RA   Zhulin I.B.;
RT   "Azospirillum genomes reveal transition of bacteria from aquatic to
RT   terrestrial environments.";
RL   PLoS Genet. 7:E1002430-E1002430(2011).
CC   -!- SIMILARITY: Belongs to the thioredoxin family.
CC       {ECO:0000256|ARBA:ARBA00008987}.
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DR   EMBL; FQ311872; CBS90567.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7ZGW5; -.
DR   KEGG; ali:AZOLI_p40170; -.
DR   HOGENOM; CLU_090389_10_0_5; -.
DR   OMA; NPCRMLT; -.
DR   OrthoDB; 9790390at2; -.
DR   Proteomes; UP000005667; Plasmid AZO_p4.
DR   GO; GO:0015035; F:protein-disulfide reductase activity; IEA:InterPro.
DR   CDD; cd02947; TRX_family; 1.
DR   Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR   Gene3D; 2.30.30.380; Zn-finger domain of Sec23/24; 1.
DR   InterPro; IPR049299; Thio2_N.
DR   InterPro; IPR005746; Thioredoxin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   InterPro; IPR017937; Thioredoxin_CS.
DR   InterPro; IPR013766; Thioredoxin_domain.
DR   NCBIfam; TIGR01068; thioredoxin; 1.
DR   PANTHER; PTHR45663; GEO12009P1; 1.
DR   PANTHER; PTHR45663:SF11; GEO12009P1; 1.
DR   Pfam; PF21352; Thio2_N; 1.
DR   Pfam; PF00085; Thioredoxin; 1.
DR   PRINTS; PR00421; THIOREDOXIN.
DR   SUPFAM; SSF52833; Thioredoxin-like; 1.
DR   PROSITE; PS00194; THIOREDOXIN_1; 1.
DR   PROSITE; PS51352; THIOREDOXIN_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Plasmid {ECO:0000313|EMBL:CBS90567.1};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284};
KW   Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   DOMAIN          58..163
FT                   /note="Thioredoxin"
FT                   /evidence="ECO:0000259|PROSITE:PS51352"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   164 AA;  17361 MW;  C1EB798B4CB902C1 CRC64;
     MPTTAQSSGH SSTGTQSSTG ADSLHVACPH CDTLNRVPTA RLGGGKCGRC GKPLFEGKPV
     ALDASRFAAH AERGDLPLLI DFWADWCGPC RMMAPVFAQA AAQLEPRLRL AKIDTEASPD
     LAARFGIRSI PSLVLVHHGR EIARTAGAMP LPALVGWVRQ TLGR
//
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